During the course of these studies, we intend to evaluate some structural analogues of L-Lysine, as antifibrinolytic agents, and as ligands which produce a conformation alteration in human plasminogen. The analogues are cis-4,5-lysene, trans-4,5-lysene and lysyne. We will measure the binding of each of these amino acids to human plasminogen, by monitoring the well-known alteration in the intrinsic fluorescence and sedimentation of human plasminogen which they produce. We will also compare the relative effectiveness of these amino acids in stimulating the conversion of Glu-plasminogen to Glu-plasmin, Glu-plasminogen to Lys-plasminogen to Glu-plasmin, Glu-plasminogen to Lys-plasminogen, and Glu-plasmin to Lys-plasmin. We also intend to perform metabolic studies on plasminogen isozymes and the multiple forms of the isozymes. We will determine the individual rates of synthesis, degradation, and potential interconversions of the 2 major forms of rat plasminogen in germ-free rats. Additionally, we intend to determine the rates of synthesis, degradation, and potential interconversions of the subforms of the 2 major plasminogen forms in conventional animals. Finally, we will compare physical and kinetic and activation properties of the various multiple forms of human plasminogen and the corresponding plasmins.